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Molecular Pharmacology Fast Forward
First published on August 3, 2006; DOI: 10.1124/mol.106.027029

0026-895X/06/7005-1469-1480$20.00
Mol Pharmacol 70:1469-1480, 2006

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Hypoxia-Inducible Factor-1 (HIF-1)

Qingdong Ke, and Max Costa

Nelson Institute of Environmental Medicine, New York University, School of Medicine, Tuxedo, New York

Adaptation to low oxygen tension (hypoxia) in cells and tissues leads to the transcriptional induction of a series of genes that participate in angiogenesis, iron metabolism, glucose metabolism, and cell proliferation/survival. The primary factor mediating this response is the hypoxia-inducible factor-1 (HIF-1), an oxygen-sensitive transcriptional activator. HIF-1 consists of a constitutively expressed subunit HIF-1beta and an oxygen-regulated subunit HIF-1{alpha} (or its paralogs HIF-2{alpha} and HIF-3{alpha}). The stability and activity of the {alpha} subunit of HIF are regulated by its post-translational modifications such as hydroxylation, ubiquitination, acetylation, and phosphorylation. In normoxia, hydroxylation of two proline residues and acetylation of a lysine residue at the oxygen-dependent degradation domain (ODDD) of HIF-1{alpha} trigger its association with pVHL E3 ligase complex, leading to HIF-1{alpha} degradation via ubiquitin-proteasome pathway. In hypoxia, the HIF-1{alpha} subunit becomes stable and interacts with coactivators such as cAMP response element-binding protein binding protein/p300 and regulates the expression of target genes. Overexpression of HIF-1 has been found in various cancers, and targeting HIF-1 could represent a novel approach to cancer therapy.

Received May 25, 2006; accepted August 2, 2006

Address correspondence to: Dr. Max Costa, Nelson Institute of Environmental Medicine, New York University School of Medicine, 57 Old Forge Road, Tuxedo, NY 10987. E-mail: costam01{at}nyu.edu




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